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P46840 (CTPB_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cation-transporting P-type ATPase B
EC=3.6.3.-
Gene names
Name:ctpB
Ordered Locus Names:ML2000
OrganismMycobacterium leprae [Complete proteome] [HAMAP]
Taxonomic identifier1769 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper-exporting ATPase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 750750Cation-transporting P-type ATPase B
PRO_0000046167

Regions

Transmembrane104 – 12421Helical; Potential
Transmembrane129 – 14921Helical; Potential
Transmembrane167 – 18721Helical; Potential
Transmembrane200 – 22021Helical; Potential
Transmembrane360 – 38021Helical; Potential
Transmembrane389 – 40921Helical; Potential
Transmembrane471 – 49121Helical; Potential
Transmembrane500 – 52021Helical; Potential
Transmembrane547 – 56721Helical; Potential
Transmembrane663 – 68321Helical; Potential
Transmembrane693 – 71321Helical; Potential
Transmembrane715 – 73521Helical; Potential
Domain18 – 8164HMA

Sites

Active site44514-aspartylphosphate intermediate Probable
Metal binding281 Potential
Metal binding311 Potential

Experimental info

Sequence conflict544 – 5485EGESR → RRRIT in CAA86363. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46840 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 1D58477D4A69B00D

FASTA75078,101
        10         20         30         40         50         60 
MTASLVEDTN NNHESVRRIQ LDVAGMLCAA CASRVETKLN KIPGVRASVN FATRVATIDA 

        70         80         90        100        110        120 
VDVAVDELRQ VIEQAGYRAT AHAESAVEEI DPDADYARNL LRRLIVAALL FVPLADLSTM 

       130        140        150        160        170        180 
FAIVPTNRFP GWGYLLTALA APIVTWAAWP FHRVALRNAR YRAASMETLI SAGILAATGW 

       190        200        210        220        230        240 
SLSTIFVDKE PRQTHGIWQA ILHSDSIYFE VAAGVTVFVL AGRFFEARAK SKAGSALRAL 

       250        260        270        280        290        300 
AARGAKNVEV LLPNGAELTI PAGELKKQQH FLVRPGETIT ADGVVIDGTA TIDMSAITGE 

       310        320        330        340        350        360 
ARPVHASPAS TVVGGTTVLD GRLVIEATAV GGDTQFAAMV RLVEDAQVQK ARVQHLADRI 

       370        380        390        400        410        420 
AAVFVPMVFV IAGLAGASWL LAGASPDRAF SVVLGVLVIA CPCTLGLATP TAMMVASGRG 

       430        440        450        460        470        480 
AQLGIFIKGY RALETINAID TVVFDKTGTL TLGQLSVSTV TSTGGWCSGE VLALASAVEA 

       490        500        510        520        530        540 
ASEHSVATAI VAAYADPRPV ADFVAFAGCG VSGVVAEHHV KIGKPSWVTR NAPCDVVLES 

       550        560        570        580        590        600 
ARREGESRGE TVVFVSVDGV ACGAVAIADT VKDSAADAIS ALCSRGLHTI LLTGDNQAAA 

       610        620        630        640        650        660 
RAVAAQVGID TVIADMLPEA KVDVIQRLRD QGHTVAMVGD GINDGPALAC ADLGLAMGRG 

       670        680        690        700        710        720 
TDVAIGAADL ILVRDSLGVV PVALDLARAT MRTIRINMIW AFGYNVAAIP IASSGLLNPL 

       730        740        750 
IAGAAMAFSS FFVVSNSLRL SNFGLSQTSD

« Hide

References

« Hide 'large scale' references
[1]"The Mycobacterium leprae genome: systematic sequence analysis identifies key catabolic enzymes, ATP-dependent transport systems and a novel polA locus associated with genomic variability."
Fsihi H., Cole S.T.
Mol. Microbiol. 16:909-919(1995) [PubMed: 7476188] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Massive gene decay in the leprosy bacillus."
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. expand/collapse author list , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G.
Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z46257 Genomic DNA. Translation: CAA86363.1.
AL583924 Genomic DNA. Translation: CAC30955.1.
PIRC87159.
S77653.
RefSeqNP_302350.1. NC_002677.1.

3D structure databases

ProteinModelPortalP46840.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000028292; EBMYCP00000027898; EBMYCG00000028287.
GeneID909077.
GenomeReviewsGene locus ML2000 in contig AL450380_GR.
KEGGmle:ML2000.
NMPDRfig|272631.1.peg.1222.
PATRIC18057672. VBIMycLep78757_3760.

Organism-specific databases

LepromaML2000.
CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016190.
HOGENOMHBG507745.
OMAHAESQGH.
ProtClustDBCLSK790257.

Enzyme and pathway databases

BioCycMLEP272631:ML2000-MONOMER.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR000579. ATPase_P-typ_cation-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK12949.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00940. CATPATPASEA.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCTPB_MYCLE
AccessionPrimary (citable) accession number: P46840
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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